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Literature summary for 2.3.1.35 extracted from

  • Dou, W.; Xu, M.; Cai, D.; Zhang, X.; Rao, Z.; Xu, Z.
    Improvement of L-arginine production by overexpression of a bifunctional ornithine acetyltransferase in Corynebacterium crenatum (2011), Appl. Biochem. Biotechnol., 165, 845-855.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Corynebacterium crenatum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39700
-
calculated from cDNA Corynebacterium crenatum

Organism

Organism UniProt Comment Textmining
Corynebacterium crenatum C1KGU6 functional study reveals that OATase from Corynebacterium crenatum SYPA5-5 is a bifunctional enzyme with the functions of acetylglutamate synthase and acetylornithine deacetylase
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N2-acetyl-L-ornithine + L-glutamate
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Corynebacterium crenatum L-ornithine + N-acetyl-L-glutamate
-
?

Subunits

Subunits Comment Organism
heterodimer alpha- and beta-subunits can not self-assemble to active OATase conformation Corynebacterium crenatum

Synonyms

Synonyms Comment Organism
argJ
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Corynebacterium crenatum
OATase
-
Corynebacterium crenatum
ornithine acetyltransferase
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Corynebacterium crenatum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Corynebacterium crenatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Corynebacterium crenatum

General Information

General Information Comment Organism
metabolism overexpression of a OTase in Corynebacterium crenatum leads to an improvement of L-Arginine production Corynebacterium crenatum